A fresh trim provides a new look at the human mannose receptor

The human mannose receptor plays an important role in scavenging a variety of glycans and glycoconjugates, which contributes to both innate and adaptive immunity. However, the fine details of its ligand specificity, and specifically that of carbohydrate-recognition domain 4, the most functionally relevant C-type lectin domain within the receptor, are not completely understood. Feinberg et al. use glycan arrays, crystallography, and a newly trimmed version of carbohydrate-recognition domain 4 to elucidate the molecular mechanisms driving binding specificity. These data contribute to our molecular understanding of Ca2+-mediated binding promiscuity in the human mannose receptor and the scavenging role of the receptor itself and highlight unexpected interactions that should inspire further study.

Automated summary

The study investigates the ligand specificity of the human mannose receptor, particularly focusing on carbohydrate-recognition domain 4, and elucidates the molecular mechanisms driving binding specificity. The data contribute to understanding Ca2+-mediated binding promiscuity in the receptor and highlight unexpected interactions for further study.